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Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)

Membrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by...

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Autores principales: Guzmán-Flores, José E., Steinemann-Hernández, Lidia, González de la Vara, Luis E., Gavilanes-Ruiz, Marina, Romeo, Tony, Alvarez, Adrián F., Georgellis, Dimitris
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6788730/
https://www.ncbi.nlm.nih.gov/pubmed/31603938
http://dx.doi.org/10.1371/journal.pone.0223794
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author Guzmán-Flores, José E.
Steinemann-Hernández, Lidia
González de la Vara, Luis E.
Gavilanes-Ruiz, Marina
Romeo, Tony
Alvarez, Adrián F.
Georgellis, Dimitris
author_facet Guzmán-Flores, José E.
Steinemann-Hernández, Lidia
González de la Vara, Luis E.
Gavilanes-Ruiz, Marina
Romeo, Tony
Alvarez, Adrián F.
Georgellis, Dimitris
author_sort Guzmán-Flores, José E.
collection PubMed
description Membrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by mass spectrometry analyses of Detergent Resistant Membranes (DRM). We report that at least three of the four E. coli flotillin homologous proteins were found to reside in DRM, along with 77 more proteins. Moreover, the proteomic data were validated by subcellular localization, using immunoblot assays and fluorescence microscopy of selected proteins. Our results confirm the existence of lipid raft-like microdomains in the inner membrane of E. coli and represent the first comprehensive profiling of proteins in these bacterial membrane platforms.
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spelling pubmed-67887302019-10-25 Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM) Guzmán-Flores, José E. Steinemann-Hernández, Lidia González de la Vara, Luis E. Gavilanes-Ruiz, Marina Romeo, Tony Alvarez, Adrián F. Georgellis, Dimitris PLoS One Research Article Membrane microdomains or lipid rafts compartmentalize cellular processes by laterally organizing membrane components. Such sub-membrane structures were mainly described in eukaryotic cells, but, recently, also in bacteria. Here, the protein content of lipid rafts in Escherichia coli was explored by mass spectrometry analyses of Detergent Resistant Membranes (DRM). We report that at least three of the four E. coli flotillin homologous proteins were found to reside in DRM, along with 77 more proteins. Moreover, the proteomic data were validated by subcellular localization, using immunoblot assays and fluorescence microscopy of selected proteins. Our results confirm the existence of lipid raft-like microdomains in the inner membrane of E. coli and represent the first comprehensive profiling of proteins in these bacterial membrane platforms. Public Library of Science 2019-10-11 /pmc/articles/PMC6788730/ /pubmed/31603938 http://dx.doi.org/10.1371/journal.pone.0223794 Text en © 2019 Guzmán-Flores et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Guzmán-Flores, José E.
Steinemann-Hernández, Lidia
González de la Vara, Luis E.
Gavilanes-Ruiz, Marina
Romeo, Tony
Alvarez, Adrián F.
Georgellis, Dimitris
Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)
title Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)
title_full Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)
title_fullStr Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)
title_full_unstemmed Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)
title_short Proteomic analysis of Escherichia coli detergent-resistant membranes (DRM)
title_sort proteomic analysis of escherichia coli detergent-resistant membranes (drm)
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6788730/
https://www.ncbi.nlm.nih.gov/pubmed/31603938
http://dx.doi.org/10.1371/journal.pone.0223794
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